4.7 Article

Action spectroscopy of the isolated red Kaede fluorescent protein chromophore

Journal

JOURNAL OF CHEMICAL PHYSICS
Volume 155, Issue 12, Pages -

Publisher

AIP Publishing
DOI: 10.1063/5.0063258

Keywords

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Funding

  1. Swedish Foundation for International Cooperation in Research and Higher Education (STINT) Grant for Internationalisation program [PT2017-7328]
  2. University of East Anglia
  3. NSERC
  4. province of Ontario
  5. Swedish Research Council [2016-03675]
  6. Olle Engkvist Foundation [200-575]
  7. Ministerio de Ciencia, Innovacion y Universidades (Spain) [PID-2019-104654GBI00]
  8. Novo Nordisk Foundation [NNF20OC0064958]
  9. EPSRC [EP/H025715/1]
  10. Research and Specialist Computing Support service at the University of East Anglia
  11. EPSRC [EP/H025715/1] Funding Source: UKRI
  12. Swedish Research Council [2016-03675] Funding Source: Swedish Research Council

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Incorporation of fluorescent proteins into biochemical systems has revolutionized bioimaging. A study on the red Kaede fluorescent protein chromophore in the gas phase revealed three isomers, highlighting the need for isomer-selective methods in studying biochromophores.
Incorporation of fluorescent proteins into biochemical systems has revolutionized the field of bioimaging. In a bottom-up approach, understanding the photophysics of fluorescent proteins requires detailed investigations of the light-absorbing chromophore, which can be achieved by studying the chromophore in isolation. This paper reports a photodissociation action spectroscopy study on the deprotonated anion of the red Kaede fluorescent protein chromophore, demonstrating that at least three isomers-assigned to deprotomers-are generated in the gas phase. Deprotomer-selected action spectra are recorded over the S-1 & LARR; S-0 band using an instrument with differential mobility spectrometry coupled with photodissociation spectroscopy. The spectrum for the principal phenoxide deprotomer spans the 480-660 nm range with a maximum response at & AP;610 nm. The imidazolate deprotomer has a blue-shifted action spectrum with a maximum response at & AP;545 nm. The action spectra are consistent with excited state coupled-cluster calculations of excitation wavelengths for the deprotomers. A third gas-phase species with a distinct action spectrum is tentatively assigned to an imidazole tautomer of the principal phenoxide deprotomer. This study highlights the need for isomer-selective methods when studying the photophysics of biochromophores possessing several deprotonation sites.

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